Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism

Urbanowicz, Breeanna R.; Bharadwaj, Vivek S.; Alahuhta, Markus; Pena, Maria J.; Lunin, Vladimir V.; Bomble, Yannick J.; Wang, Shuo; Yang, Jeong -Yeh; Tuomivaara, Sami T.; Himmel, Michael E.; Moremen, Kelley W.; York, William S.; Crowley, Michael F.

doi:10.1111/tpj.13628

Title: Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism

Journal Article · Mon Jul 03 00:00:00 EDT 2017 · The Plant Journal

DOI:https://doi.org/10.1111/tpj.13628· OSTI ID:1389734

Urbanowicz, Breeanna R. ^[1];

^[2]; Alahuhta, Markus ^[2]; Pena, Maria J. ^[1]; Lunin, Vladimir V. ^[2]; Bomble, Yannick J. ^[2]; Wang, Shuo ^[1]; Yang, Jeong -Yeh ^[1]; Tuomivaara, Sami T. ^[3]; Himmel, Michael E. ^[2]; Moremen, Kelley W. ^[1]; York, William S. ^[1]; Crowley, Michael F. ^[2]

Univ. of Georgia, Athens, GA (United States)
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Univ. of Georgia, Athens, GA (United States); Univ. of California San Francisco, San Francisco, CA (United States)

Summary The mechanistic underpinnings of the complex process of plant polysaccharide biosynthesis are poorly understood, largely because of the resistance of glycosyltransferase (GT) enzymes to structural characterization. In Arabidopsis thaliana, a glycosyl transferase family 37 (GT37) fucosyltransferase 1 ( At FUT1) catalyzes the regiospecific transfer of terminal 1,2‐fucosyl residues to xyloglucan side chains – a key step in the biosynthesis of fucosylated sidechains of galactoxyloglucan. We unravel the mechanistic basis for fucosylation by At FUT1 with a multipronged approach involving protein expression, X‐ray crystallography, mutagenesis experiments and molecular simulations. Mammalian cell culture expressions enable the sufficient production of the enzyme for X‐ray crystallography, which reveals the structural architecture of At FUT1 in complex with bound donor and acceptor substrate analogs. The lack of an appropriately positioned active site residue as a catalytic base leads us to propose an atypical water‐mediated fucosylation mechanism facilitated by an H‐bonded network, which is corroborated by mutagenesis experiments as well as detailed atomistic simulations.

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Research Organization:: National Renewable Energy Laboratory (NREL), Golden, CO (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Energy Efficiency and Renewable Energy (EERE)

Grant/Contract Number:: AC36-08GO28308

OSTI ID:: 1389734

Alternate ID(s):: OSTI ID: 1377643

Report Number(s):: NREL/JA-2700-67766

Journal Information:: The Plant Journal, Vol. 91, Issue 6; ISSN 0960-7412

Publisher:: Society for Experimental BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 41 works

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